Q3V7T4 (THD1_STAAS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Threonine dehydratase biosynthetic
EC=4.3.1.19

Alternative name(s):
Threonine deaminase

Gene names

Name:	ilvA
Ordered Locus Names:	SAS1966

Organism

Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP]

Taxonomic identifier

282459 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the formation of alpha-ketobutyrate from threonine in a two-step reaction. The first step is a dehydration of threonine, followed by rehydration and liberation of ammonia By similarity.
Catalytic activity	L-threonine = 2-oxobutanoate + NH3.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
Sequence similarities	Belongs to the serine/threonine dehydratase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-threonine ammonia-lyase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 422	422	Threonine dehydratase biosynthetic		PRO_0000234310
Amino acid modifications
	Modified residue	56	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3V7T4 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: D57A860757C56CD5	FASTA	422	46,967
	10 20 30 40 50 60 MTVKTTVSTK DIDEAFLRLK DIVKETPLQL DHYLSQKYDC KVYLKREDLQ WVRSFKLRGA 70 80 90 100 110 120 YNAISVLSDE AKSKGITCAS AGNHAQGVAY TAKKLNLNAV IFMPVTTPLQ KVNQVKFFGN 130 140 150 160 170 180 SNVEVVLTGD TFDHCLAEAL TYTSEHQMNF IDPFNNVHTI SGQGTLAKEM LEQSKTDNVN 190 200 210 220 230 240 FDYLFAAIGG GGLISGISTY FKTYSPTTKI IGVEPSGASS MYESVVVNNQ VVTLPNIDKF 250 260 270 280 290 300 VDGASVARVG DITFEIAKEN VDDYVQVDEG AVCSTILDMY SKQAIVAEPA GALSVSALEN 310 320 330 340 350 360 YKDHIKGKTV VCVISGGNND INRMKEIEER SLLYEEMKHY FILNFPQRPG ALREFVNDVL 370 380 390 400 410 420 GPQDDITKFE YLKKSSQNTG TVIIGIQLKD HDDLIQLKQR VNHFDPSNIY INENKMLYSL LI

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MSSA476.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571857 Genomic DNA. Translation: CAG43773.1.
RefSeq	YP_044076.1. NC_002953.3.
3D structure databases
ProteinModelPortal	Q3V7T4.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3V7T4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000023332; EBSTAP00000022499; EBSTAG00000023331.
GeneID	2861792.
GenomeReviews	Gene locus SAS1966 in contig BX571857_GR.
KEGG	sas:SAS1966.
PATRIC	19553531. VBIStaAur96780_2047.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1171.
GeneTree	EBGT00050000024421.
HOGENOM	HBG714501.
OMA	IYIAVGG.
PhylomeDB	Q3V7T4.
ProtClustDB	PRK08639.
Enzyme and pathway databases
BioCyc	SAUR282459:SAS1966-MONOMER.
Family and domain databases
InterPro	IPR001926. PyrdxlP-dep_enz_bsu. IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR001721. Thr_deHydtase_C. IPR011820. Threonine_deHydtase. [Graphical view]
KO	K01754.
Pfam	PF00291. PALP. 1 hit. PF00585. Thr_dehydrat_C. 1 hit. [Graphical view]
SUPFAM	SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMs	TIGR02079. THD1. 1 hit.
PROSITE	PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THD1_STAAS

Accession

Primary (citable) accession number: Q3V7T4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	October 11, 2005
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program